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R1AB_IBVBC
ID   R1AB_IBVBC              Reviewed;        6629 AA.
AC   P0C6Y2; Q91QT2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Replicase polyprotein 1ab;
DE            Short=pp1ab;
DE   AltName: Full=ORF1ab polyprotein;
DE   Contains:
DE     RecName: Full=Non-structural protein 2;
DE              Short=nsp2;
DE     AltName: Full=p87;
DE   Contains:
DE     RecName: Full=Papain-like protease;
DE              Short=PL-PRO;
DE              EC=3.4.19.12 {ECO:0000250|UniProtKB:P0C6X7};
DE              EC=3.4.22.- {ECO:0000250|UniProtKB:P0C6X7};
DE     AltName: Full=Non-structural protein 3;
DE              Short=nsp3;
DE     AltName: Full=p195;
DE   Contains:
DE     RecName: Full=Non-structural protein 4;
DE              Short=nsp4;
DE     AltName: Full=Peptide HD2;
DE     AltName: Full=p41;
DE   Contains:
DE     RecName: Full=3C-like proteinase;
DE              Short=3CL-PRO;
DE              Short=3CLp;
DE              EC=3.4.22.- {ECO:0000250|UniProtKB:P0C6X7};
DE     AltName: Full=Main protease;
DE              Short=Mpro;
DE     AltName: Full=Non-structural protein 5;
DE              Short=nsp5;
DE     AltName: Full=p33;
DE   Contains:
DE     RecName: Full=Non-structural protein 6;
DE              Short=nsp6;
DE     AltName: Full=p34;
DE   Contains:
DE     RecName: Full=Non-structural protein 7;
DE              Short=nsp7;
DE     AltName: Full=p9;
DE   Contains:
DE     RecName: Full=Non-structural protein 8;
DE              Short=nsp8;
DE     AltName: Full=p24;
DE   Contains:
DE     RecName: Full=Non-structural protein 9;
DE              Short=nsp9;
DE     AltName: Full=p10;
DE   Contains:
DE     RecName: Full=Non-structural protein 10;
DE              Short=nsp10;
DE     AltName: Full=Growth factor-like peptide;
DE              Short=GFL;
DE     AltName: Full=p16;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              Short=Pol;
DE              Short=RdRp;
DE              EC=2.7.7.48;
DE     AltName: Full=nsp12;
DE     AltName: Full=p100;
DE   Contains:
DE     RecName: Full=Helicase;
DE              Short=Hel;
DE              EC=3.6.4.12 {ECO:0000250|UniProtKB:P0C6X7};
DE              EC=3.6.4.13 {ECO:0000250|UniProtKB:P0C6X7};
DE     AltName: Full=nsp13;
DE     AltName: Full=p68;
DE   Contains:
DE     RecName: Full=Proofreading exoribonuclease {ECO:0000250|UniProtKB:P0C6X7};
DE              Short=ExoN;
DE              EC=2.1.1.-;
DE              EC=3.1.13.-;
DE     AltName: Full=Guanine-N7 methyltransferase {ECO:0000250|UniProtKB:P0C6X7};
DE     AltName: Full=Non-structural protein 14;
DE              Short=nsp14;
DE     AltName: Full=p58;
DE   Contains:
DE     RecName: Full=Uridylate-specific endoribonuclease;
DE              EC=4.6.1.- {ECO:0000250|UniProtKB:P0C6X7};
DE     AltName: Full=NendoU;
DE     AltName: Full=Non-structural protein 15;
DE              Short=nsp15;
DE     AltName: Full=p39;
DE   Contains:
DE     RecName: Full=2'-O-methyl transferase;
DE              EC=2.1.1.57;
DE     AltName: Full=Non-structural protein 16;
DE              Short=nsp16;
DE     AltName: Full=p35;
GN   Name=rep; ORFNames=1a-1b;
OS   Avian infectious bronchitis virus (strain Beaudette CK) (IBV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Gammacoronavirus; Igacovirus.
OX   NCBI_TaxID=160235;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Casais R., Thiel V., Siddell S., Cavanagh D., Britton P.;
RT   "Recovery of the avian coronavirus infectious bronchitis virus from cDNA
RT   assembled in vaccinia virus.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: [Isoform Replicase polyprotein 1ab]: Multifunctional protein
CC       involved in the transcription and replication of viral RNAs. Contains
CC       the proteinases responsible for the cleavages of the polyprotein.
CC       {ECO:0000305}.
CC   -!- FUNCTION: [Non-structural protein 2]: May play a role in the modulation
CC       of host cell survival signaling pathway by interacting with host PHB
CC       and PHB2 (By similarity). Indeed, these two proteins play a role in
CC       maintaining the functional integrity of the mitochondria and protecting
CC       cells from various stresses (By similarity).
CC       {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- FUNCTION: [Papain-like protease]: Responsible for the cleavages located
CC       at the N-terminus of the replicase polyprotein (By similarity). In
CC       addition, PL-PRO possesses a deubiquitinating/deISGylating activity and
CC       processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from
CC       cellular substrates (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- FUNCTION: [Non-structural protein 4]: Plays a role in host membrane
CC       rearrangement that leads to creation of cytoplasmic double-membrane
CC       vesicles (DMV) necessary for viral replication (By similarity). Alone
CC       is able to induce paired membranes (By similarity). Coexpression of
CC       nsp3 and nsp4 does not result in the formation of DMVs (By similarity).
CC       {ECO:0000250|UniProtKB:P0C6Y3}.
CC   -!- FUNCTION: [3C-like proteinase]: Responsible for the majority of
CC       cleavages as it cleaves the C-terminus of replicase polyprotein at 11
CC       sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-
CC       [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-
CC       CMK. {ECO:0000255|PROSITE-ProRule:PRU00772}.
CC   -!- FUNCTION: [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8
CC       subunits of each) that may participate in viral replication by acting
CC       as a primase. Alternatively, may synthesize substantially longer
CC       products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- FUNCTION: [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8
CC       subunits of each) that may participate in viral replication by acting
CC       as a primase. Alternatively, may synthesize substantially longer
CC       products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- FUNCTION: [Non-structural protein 9]: Plays an essential role in viral
CC       replication by forming a homodimer that binds single-stranded RNA.
CC       {ECO:0000250|UniProtKB:P0C6Y3}.
CC   -!- FUNCTION: [Non-structural protein 10]: Plays a pivotal role in viral
CC       transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16
CC       2'-O-methyltransferase activities (By similarity). Therefore plays an
CC       essential role in viral mRNAs cap methylation (By similarity).
CC       {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- FUNCTION: [RNA-directed RNA polymerase]: Responsible for replication
CC       and transcription of the viral RNA genome.
CC       {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- FUNCTION: [Helicase]: Multi-functional protein with a zinc-binding
CC       domain in N-terminus displaying RNA and DNA duplex-unwinding activities
CC       with 5' to 3' polarity. Activity of helicase is dependent on magnesium.
CC       {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- FUNCTION: [Proofreading exoribonuclease]: Enzyme possessing two
CC       different activities: an exoribonuclease activity acting on both ssRNA
CC       and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase
CC       activity (By similarity). Acts as a proofreading exoribonuclease for
CC       RNA replication, thereby lowering The sensitivity of the virus to RNA
CC       mutagens (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- FUNCTION: [Uridylate-specific endoribonuclease]: Plays a role in viral
CC       transcription/replication and prevents the simultaneous activation of
CC       host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By
CC       similarity). Acts by degrading the 5'-polyuridines generated during
CC       replication of the poly(A) region of viral genomic and subgenomic RNAs
CC       (By similarity). Catalyzes a two-step reaction in which a 2'3'-cyclic
CC       phosphate (2'3'-cP) is first generated by 2'-O transesterification,
CC       which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If
CC       not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and
CC       activate host dsRNA sensors (By similarity).
CC       {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- FUNCTION: [2'-O-methyl transferase]: Methyltransferase that mediates
CC       mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral
CC       mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16.
CC       Therefore plays an essential role in viral mRNAs cap methylation which
CC       is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY: [Helicase]:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC   -!- CATALYTIC ACTIVITY: [Helicase]:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC   -!- CATALYTIC ACTIVITY: [Papain-like protease]:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:P0C6Y1};
CC   -!- CATALYTIC ACTIVITY: [Uridylate-specific endoribonuclease]:
CC       Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-
CC         2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-
CC         RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-
CC         COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284,
CC         ChEBI:CHEBI:173079, ChEBI:CHEBI:173080;
CC         Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC   -!- CATALYTIC ACTIVITY: [2'-O-methyl transferase]:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC         in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC         Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC         EC=2.1.1.57; Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC   -!- COFACTOR: [Uridylate-specific endoribonuclease]:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC       Note=Likely affects Nsp15 binding to RNA.
CC       {ECO:0000250|UniProtKB:P0C6X7};
CC   -!- COFACTOR: [Papain-like protease]:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC   -!- SUBUNIT: [Non-structural protein 2]: Interacts with host PHB and PHB2.
CC       {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- SUBUNIT: [Non-structural protein 4]: Interacts with papain-like
CC       protease and non-structural protein 6. {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- SUBUNIT: [3C-like proteinase]: Monomer. Homodimer. Only the homodimer
CC       shows catalytic activity. {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- SUBUNIT: [Non-structural protein 7]: Eight copies of nsp7 and eight
CC       copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling
CC       ring structure. {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- SUBUNIT: [Non-structural protein 8]: Eight copies of nsp7 and eight
CC       copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling
CC       ring structure (By similarity). Interacts with ORF6 protein (By
CC       similarity). {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- SUBUNIT: [Non-structural protein 9]: Homodimer.
CC       {ECO:0000250|UniProtKB:P0C6Y3}.
CC   -!- SUBUNIT: [Non-structural protein 10]: Homododecamer (By similarity).
CC       Interacts with proofreading exoribonuclease nsp14 and 2'-O-
CC       methyltransferase nsp16; these interactions enhance nsp14 and nsp16
CC       enzymatic activities (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- SUBUNIT: [Proofreading exoribonuclease]: Interacts with host DDX1 (via
CC       C-terminus) (By similarity). Interacts with non-structural protein 10
CC       (By similarity). {ECO:0000250|UniProtKB:P0C6Y1}.
CC   -!- SUBUNIT: [Uridylate-specific endoribonuclease]: Homohexamer.
CC       {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- SUBUNIT: [2'-O-methyl transferase]: Interacts with non-structural
CC       protein 10. {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- SUBCELLULAR LOCATION: [Papain-like protease]: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane
CC       protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}.
CC       Note=Gammacoronaviruses induce membrane zippering to form zippered
CC       endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane
CC       protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}.
CC       Note=Localizes in virally-induced cytoplasmic double-membrane vesicles
CC       (By similarity). Gammacoronaviruses induce membrane zippering to form
CC       zippered endoplasmic reticulum (zER) (By similarity).
CC       {ECO:0000250|UniProtKB:P0C6X7, ECO:0000250|UniProtKB:P0C6Y3}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 6]: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane
CC       protein {ECO:0000305}. Note=Gammacoronaviruses induce membrane
CC       zippering to form zippered endoplasmic reticulum (zER).
CC       {ECO:0000250|UniProtKB:P0C6Y3}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host
CC       perinuclear region {ECO:0000250}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC       localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC       they merge into confluent complexes.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host
CC       perinuclear region {ECO:0000250|UniProtKB:P0C6X7}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC       localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC       they merge into confluent complexes.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 9]: Host cytoplasm, host
CC       perinuclear region {ECO:0000250}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC       localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC       they merge into confluent complexes.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host
CC       perinuclear region {ECO:0000250}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC       localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC       they merge into confluent complexes.
CC   -!- SUBCELLULAR LOCATION: [Helicase]: Host endoplasmic reticulum-Golgi
CC       intermediate compartment {ECO:0000305}. Note=The helicase interacts
CC       with the N protein in membranous complexes and colocalizes with sites
CC       of synthesis of new viral RNA.
CC   -!- SUBCELLULAR LOCATION: [Proofreading exoribonuclease]: Host cytoplasm
CC       {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P0DTD1}.
CC   -!- SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease]: Host
CC       cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P0DTD1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC         Comment=Isoform Replicase polyprotein 1ab is produced by -1 ribosomal
CC         frameshifting at the 1a-1b genes boundary. Isoform Replicase
CC         polyprotein 1a is produced by conventional translation.
CC         {ECO:0000305};
CC       Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC         IsoId=P0C6Y2-1; Sequence=Displayed;
CC       Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC         IsoId=P0C6V4-1; Sequence=External;
CC   -!- DOMAIN: [Papain-like protease]: The hydrophobic region HD1 probably
CC       mediates the membrane association of the replication complex.
CC       {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- DOMAIN: [Non-structural protein 4]: The hydrophobic region HD2 probably
CC       mediates the membrane association of the replication complex.
CC       {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- DOMAIN: [Non-structural protein 6]: The hydrophobic region HD3 probably
CC       mediates the membrane association of the replication complex.
CC       {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- PTM: [Isoform Replicase polyprotein 1ab]: Specific enzymatic cleavages
CC       in vivo by its own proteases yield mature proteins (By similarity). 3C-
CC       like proteinase nsp5 liberates nsps 6-16 from the polyprotein (By
CC       similarity). Papain-like and 3C-like proteinases are autocatalytically
CC       processed. {ECO:0000250|UniProtKB:P0C6X7}.
CC   -!- PTM: [Non-structural protein 4]: N-glycosylated.
CC       {ECO:0000250|UniProtKB:P0C6Y1}.
CC   -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC39112.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ311317; CAC39112.1; ALT_SEQ; Genomic_RNA.
DR   SMR; P0C6Y2; -.
DR   BindingDB; P0C6Y2; -.
DR   MEROPS; C30.002; -.
DR   PRIDE; P0C6Y2; -.
DR   Proteomes; UP000114388; Genome.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004532; F:exoribonuclease activity; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   CDD; cd21409; 1B_cv_Nsp13-like; 1.
DR   CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR   CDD; cd21512; cv_gamma-delta_Nsp2_IBV-like; 1.
DR   CDD; cd21473; cv_Nsp4_TM; 1.
DR   CDD; cd21559; gammaCoV-Nsp6; 1.
DR   CDD; cd21658; gammaCoV_Nsp14; 1.
DR   CDD; cd21667; gammaCoV_Nsp5_Mpro; 1.
DR   CDD; cd21587; gammaCoV_RdRp; 1.
DR   CDD; cd21168; M_gcv_Nsp15-like; 1.
DR   CDD; cd21557; Macro_X_Nsp3-like; 1.
DR   CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR   CDD; cd21170; NTD_cv_Nsp15-like; 1.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR   Gene3D; 1.10.150.420; -; 1.
DR   Gene3D; 1.10.1840.10; -; 1.
DR   Gene3D; 1.10.8.1190; -; 1.
DR   Gene3D; 1.10.8.370; -; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   Gene3D; 2.40.10.250; -; 1.
DR   Gene3D; 2.60.120.1680; -; 1.
DR   Gene3D; 3.30.160.820; -; 1.
DR   Gene3D; 3.30.70.3540; -; 1.
DR   Gene3D; 3.40.220.10; -; 1.
DR   Gene3D; 3.40.50.11580; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR043608; CoV_NSP15_M.
DR   InterPro; IPR043606; CoV_NSP15_N.
DR   InterPro; IPR043611; CoV_NSP3_C.
DR   InterPro; IPR032505; CoV_NSP4_C.
DR   InterPro; IPR043612; CoV_NSP4_N.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR037227; EndoU-like.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR044371; Macro_X_NSP3-like.
DR   InterPro; IPR043609; NendoU_nidovirus.
DR   InterPro; IPR044863; NIRAN.
DR   InterPro; IPR036333; NSP10_sf_CoV.
DR   InterPro; IPR044343; NSP13_1B_dom_CoV.
DR   InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR   InterPro; IPR009466; NSP14_CoV.
DR   InterPro; IPR044316; NSP14_gammaCoV.
DR   InterPro; IPR044328; NSP15_gammaCoV_N.
DR   InterPro; IPR044325; NSP15_M_gammaCoV.
DR   InterPro; IPR043174; NSP15_middle_sf.
DR   InterPro; IPR042515; NSP15_N_CoV.
DR   InterPro; IPR044401; NSP15_NendoU_CoV.
DR   InterPro; IPR009461; NSP16_CoV-like.
DR   InterPro; IPR040795; NSP2_gammaCoV.
DR   InterPro; IPR044383; NSP2_IBV-like.
DR   InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR   InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR   InterPro; IPR038123; NSP4_C_sf_CoV.
DR   InterPro; IPR044308; NSP5_Mpro_GammaCoV.
DR   InterPro; IPR043610; NSP6_CoV.
DR   InterPro; IPR044368; NSP6_gammaCoV.
DR   InterPro; IPR014828; NSP7_CoV.
DR   InterPro; IPR037204; NSP7_sf_CoV.
DR   InterPro; IPR014829; NSP8_CoV.
DR   InterPro; IPR037230; NSP8_sf_CoV.
DR   InterPro; IPR014822; NSP9_CoV.
DR   InterPro; IPR036499; NSP9_sf_CoV.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013016; Peptidase_C16_CoV.
DR   InterPro; IPR008740; Peptidase_C30_CoV.
DR   InterPro; IPR043477; Peptidase_C30_dom3_CoV.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR043503; PLpro_palm_finger_dom_CoV.
DR   InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR   InterPro; IPR044358; RdRp_gammaCoV.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR009469; RNA_pol_N_CoV.
DR   InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF06471; CoV_ExoN; 1.
DR   Pfam; PF06460; CoV_Methyltr_2; 1.
DR   Pfam; PF09401; CoV_NSP10; 1.
DR   Pfam; PF19215; CoV_NSP15_C; 1.
DR   Pfam; PF19216; CoV_NSP15_M; 1.
DR   Pfam; PF19219; CoV_NSP15_N; 1.
DR   Pfam; PF19218; CoV_NSP3_C; 1.
DR   Pfam; PF16348; CoV_NSP4_C; 1.
DR   Pfam; PF19217; CoV_NSP4_N; 1.
DR   Pfam; PF19213; CoV_NSP6; 1.
DR   Pfam; PF08716; CoV_NSP7; 1.
DR   Pfam; PF08717; CoV_NSP8; 1.
DR   Pfam; PF08710; CoV_NSP9; 1.
DR   Pfam; PF08715; CoV_peptidase; 1.
DR   Pfam; PF06478; CoV_RPol_N; 1.
DR   Pfam; PF01661; Macro; 1.
DR   Pfam; PF17896; NSP2_gammaCoV; 1.
DR   Pfam; PF05409; Peptidase_C30; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   Pfam; PF01443; Viral_helicase1; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF101816; SSF101816; 1.
DR   SUPFAM; SSF140367; SSF140367; 1.
DR   SUPFAM; SSF142877; SSF142877; 1.
DR   SUPFAM; SSF143076; SSF143076; 1.
DR   SUPFAM; SSF144246; SSF144246; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF52949; SSF52949; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR   PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR   PROSITE; PS51954; COV_N7_MTASE; 1.
DR   PROSITE; PS51948; COV_NSP12_RDRP; 1.
DR   PROSITE; PS51960; COV_NSP15_NTD; 1.
DR   PROSITE; PS51992; COV_NSP3_Y3; 1.
DR   PROSITE; PS51943; COV_NSP3A_UBL; 1.
DR   PROSITE; PS51944; COV_NSP3D_UBL; 1.
DR   PROSITE; PS51946; COV_NSP4C; 1.
DR   PROSITE; PS51949; COV_NSP7; 1.
DR   PROSITE; PS51950; COV_NSP8; 1.
DR   PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1.
DR   PROSITE; PS51653; CV_ZBD; 1.
DR   PROSITE; PS51442; M_PRO; 1.
DR   PROSITE; PS51154; MACRO; 1.
DR   PROSITE; PS51958; NENDOU; 1.
DR   PROSITE; PS51947; NIRAN; 1.
DR   PROSITE; PS51955; NIV_2_O_MTASE; 1.
DR   PROSITE; PS51953; NIV_EXON; 1.
DR   PROSITE; PS51124; PEPTIDASE_C16; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   Activation of host autophagy by virus; ATP-binding; Endonuclease;
KW   Exonuclease; Helicase; Host cytoplasm; Host endoplasmic reticulum;
KW   Host membrane; Host-virus interaction; Hydrolase; Lyase; Membrane;
KW   Metal-binding; Methyltransferase; Nuclease; Nucleotide-binding;
KW   Nucleotidyltransferase; Protease; Repeat; Ribosomal frameshifting;
KW   RNA-binding; RNA-directed RNA polymerase; Thiol protease; Transferase;
KW   Transmembrane; Transmembrane helix; Viral RNA replication; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..673
FT                   /note="Non-structural protein 2"
FT                   /id="PRO_0000037418"
FT   CHAIN           674..2265
FT                   /note="Papain-like protease"
FT                   /id="PRO_0000037419"
FT   CHAIN           2266..2779
FT                   /note="Non-structural protein 4"
FT                   /id="PRO_0000037420"
FT   CHAIN           2780..3086
FT                   /note="3C-like proteinase"
FT                   /id="PRO_0000037421"
FT   CHAIN           3087..3379
FT                   /note="Non-structural protein 6"
FT                   /id="PRO_0000037422"
FT   CHAIN           3380..3462
FT                   /note="Non-structural protein 7"
FT                   /id="PRO_0000037423"
FT   CHAIN           3463..3672
FT                   /note="Non-structural protein 8"
FT                   /id="PRO_0000037424"
FT   CHAIN           3673..3783
FT                   /note="Non-structural protein 9"
FT                   /id="PRO_0000037425"
FT   CHAIN           3784..3928
FT                   /note="Non-structural protein 10"
FT                   /id="PRO_0000037426"
FT   CHAIN           3929..4868
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000037427"
FT   CHAIN           4869..5468
FT                   /note="Helicase"
FT                   /id="PRO_0000037428"
FT   CHAIN           5469..5989
FT                   /note="Proofreading exoribonuclease"
FT                   /id="PRO_0000037429"
FT   CHAIN           5990..6327
FT                   /note="Uridylate-specific endoribonuclease"
FT                   /id="PRO_0000037430"
FT   CHAIN           6328..6629
FT                   /note="2'-O-methyl transferase"
FT                   /id="PRO_0000037431"
FT   TOPO_DOM        1..1750
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   TRANSMEM        1751..1771
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1772..1843
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   TRANSMEM        1844..1864
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1865..2280
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   TRANSMEM        2281..2301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2302..2559
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   TRANSMEM        2560..2580
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2581..2611
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   TRANSMEM        2612..2632
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2633..2643
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   TRANSMEM        2644..2664
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2665..3096
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   TRANSMEM        3097..3117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3118..3121
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   TRANSMEM        3122..3142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3143..3151
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   TRANSMEM        3152..3172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3173..3188
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   TRANSMEM        3189..3209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3210..3257
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   TRANSMEM        3258..3278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3279..3296
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   TRANSMEM        3297..3317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3318..6629
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   DOMAIN          675..780
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1003..1179
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1175..1227
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1236..1497
FT                   /note="Peptidase C16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          2161..2263
FT                   /note="CoV Nsp3 Y3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   DOMAIN          2684..2779
FT                   /note="Nsp4C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT   DOMAIN          2780..3086
FT                   /note="Peptidase C30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   DOMAIN          3380..3462
FT                   /note="RdRp Nsp7 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT   DOMAIN          3463..3672
FT                   /note="RdRp Nsp8 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT   DOMAIN          3673..3783
FT                   /note="Nsp9 ssRNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT   DOMAIN          3785..3926
FT                   /note="ExoN/MTase coactivator"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   DOMAIN          3940..4198
FT                   /note="NiRAN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT   DOMAIN          4302..4868
FT                   /note="Nsp12 RNA-dependent RNA polymerase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   DOMAIN          4548..4710
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   DOMAIN          4869..4952
FT                   /note="CV ZBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   DOMAIN          5125..5305
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          5306..5477
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          5539..5753
FT                   /note="ExoN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   DOMAIN          5762..5989
FT                   /note="N7-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   DOMAIN          5990..6050
FT                   /note="Nsp15 N-terminal oligomerization"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT   DOMAIN          6051..6166
FT                   /note="AV-Nsp11N/CoV-Nsp15M"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT   DOMAIN          6183..6324
FT                   /note="NendoU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   DOMAIN          6327..6626
FT                   /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ZN_FING         1353..1390
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         3858..3878
FT                   /evidence="ECO:0000250"
FT   ZN_FING         3904..3917
FT                   /evidence="ECO:0000250"
FT   REGION          783..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1751..1864
FT                   /note="HD1"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   REGION          2281..2664
FT                   /note="HD2"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   REGION          3097..3317
FT                   /note="HD3"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   REGION          5877..5891
FT                   /note="GpppA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   ACT_SITE        1274
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1437
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1448
FT                   /note="For PL-PRO activity"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6Y1"
FT   ACT_SITE        2820
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ACT_SITE        2922
FT                   /note="For 3CL-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   ACT_SITE        4695
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        4696
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        4697
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        5557
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        5559
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        5658
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        5734
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        5739
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6212
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6227
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6267
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6371
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6455
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6499
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6532
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   BINDING         3858
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3861
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3867
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3878
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3904
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3907
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3915
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3917
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4873
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4876
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4884
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4887
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4894
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4897
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4901
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4907
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4918
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4923
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4940
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4943
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5150..5157
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         5674
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5676
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5692
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5695
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5723
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5727
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5730
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5745
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5797..5803
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         5915
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         5935
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         5946
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         5949
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   SITE            673..674
FT                   /note="Cleavage; by PL-PRO"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   SITE            2265..2266
FT                   /note="Cleavage; by PL-PRO"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   SITE            2779..2780
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   SITE            3086..3087
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   SITE            3379..3380
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   SITE            3462..3463
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   SITE            3672..3673
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   SITE            3783..3784
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   SITE            3928..3929
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   SITE            4868..4869
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   SITE            5468..5469
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   SITE            5989..5990
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT   SITE            6327..6328
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250|UniProtKB:P0C6X7"
SQ   SEQUENCE   6629 AA;  744566 MW;  887869F7EA653270 CRC64;
     MASSLKQGVS PKPRDVILVS KDIPEQLCDA LFFYTSHNPK DYADAFAVRQ KFDRSLQTGK
     QFKFETVCGL FLLKGVDKIT PGVPAKVLKA TSKLADLEDI FGVSPLARKY RELLKTACQW
     SLTVEALDVR AQTLDEIFDP TEILWLQVAA KIHVSSMAMR RLVGEVTAKV MDALGSNLSA
     LFQIVKQQIA RIFQKALAIF ENVNELPQRI AALKMAFAKC ARSITVVVVE RTLVVKEFAG
     TCLASINGAV AKFFEELPNG FMGSKIFTTL AFFKEAAVRV VENIPNAPRG TKGFEVVGNA
     KGTQVVVRGM RNDLTLLDQK ADIPVEPEGW SAILDGHLCY VFRSGDRFYA APLSGNFALS
     DVHCCERVVC LSDGVTPEIN DGLILAAIYS SFSVSELVTA LKKGEPFKFL GHKFVYAKDA
     AVSFTLAKAA TIADVLRLFQ SARVIAEDVW SSFTEKSFEF WKLAYGKVRN LEEFVKTYVC
     KAQMSIVILA AVLGEDIWHL VSQVIYKLGV LFTKVVDFCD KHWKGFCVQL KRAKLIVTET
     FCVLKGVAQH CFQLLLDAIH SLYKSFKKCA LGRIHGDLLF WKGGVHKIVQ DGDEIWFDAI
     DSVDVEDLGV VQEKSIDFEV CDDVTLPENQ PGHMVQIEDD GKNYMFFRFK KDENIYYTPM
     SQLGAINVVC KAGGKTVTFG ETTVQEIPPP DVVPIKVSIE CCGEPWNTIF KKAYKEPIEV
     DTDLTVEQLL SVIYEKMCDD LKLFPEAPEP PPFENVALVD KNGKDLDCIK SCHLIYRDYE
     SDDDIEEEDA EECDTDSGEA EECDTNSECE EEDEDTKVLA LIQDPASIKY PLPLDEDYSV
     YNGCIVHKDA LDVVNLPSGE ETFVVNNCFE GAVKPLPQKV VDVLGDWGEA VDAQEQLCQQ
     EPLQHTFEEP VENSTGSSKT MTEQVVVEDQ ELPVVEQDQD VVVYTPTDLE VAKETAEEVD
     EFILIFAVPK EEVVSQKDGA QIKQEPIQVV KPQREKKAKK FKVKPATCEK PKFLEYKTCV
     GDLTVVIAKA LDEFKEFCIV NAANEHMTHG SGVAKAIADF CGLDFVEYCE DYVKKHGPQQ
     RLVTPSFVKG IQCVNNVVGP RHGDNNLHEK LVAAYKNVLV DGVVNYVVPV LSLGIFGVDF
     KMSIDAMREA FEGCTIRVLL FSLSQEHIDY FDVTCKQKTI YLTEDGVKYR SIVLKPGDSL
     GQFGQVYAKN KIVFTADDVE DKEILYVPTT DKSILEYYGL DAQKYVIYLQ TLAQKWNVQY
     RDNFLILEWR DGNCWISSAI VLLQAAKIRF KGFLTEAWAK LLGGDPTDFV AWCYASCTAK
     VGDFSDANWL LANLAEHFDA DYTNAFLKKR VSCNCGIKSY ELRGLEACIQ PVRATNLLHF
     KTQYSNCPTC GANNTDEVIE ASLPYLLLFA TDGPATVDCD EDAVGTVVFV GSTNSGHCYT
     QAAGQAFDNL AKDRKFGKKS PYITAMYTRF AFKNETSLPV AKQSKGKSKS VKEDVSNLAT
     SSKASFDNLT DFEQWYDSNI YESLKVQESP DNFDKYVSFT TKEDSKLPLT LKVRGIKSVV
     DFRSKDGFIY KLTPDTDENS KAPVYYPVLD AISLKAIWVE GNANFVVGHP NYYSKSLHIP
     TFWENAENFV KMGDKIGGVT MGLWRAEHLN KPNLERIFNI AKKAIVGSSV VTTQCGKLIG
     KAATFIADKV GGGVVRNITD SIKGLCGITR GHFERKMSPQ FLKTLMFFLF YFLKASVKSV
     VASYKTVLCK VVLATLLIVW FVYTSNPVMF TGIRVLDFLF EGSLCGPYKD YGKDSFDVLR
     YCADDFICRV CLHDKDSLHL YKHAYSVEQV YKDAASGFIF NWNWLYLVFL ILFVKPVAGF
     VIICYCVKYL VLNSTVLQTG VCFLDWFVQT VFSHFNFMGA GFYFWLFYKI YIQVHHILYC
     KDVTCEVCKR VARSNRQEVS VVVGGRKQIV HVYTNSGYNF CKRHNWYCRN CDDYGHQNTF
     MSPEVAGELS EKLKRHVKPT AYAYHVVDEA CLVDDFVNLK YKAATPGKDS ASSAVKCFSV
     TDFLKKAVFL KEALKCEQIS NDGFIVCNTQ SAHALEEAKN AAIYYAQYLC KPILILDQAL
     YEQLVVEPVS KSVIDKVCSI LSSIISVDTA ALNYKAGTLR DALLSITKDE EAVDMAIFCH
     NHDVDYTGDG FTNVIPSYGI DTGKLTPRDR GFLINADASI ANLRVKNAPP VVWKFSELIK
     LSDSCLKYLI SATVKSGVRF FITKSGAKQV IACHTQKLLV EKKAGGIVSG TFKCFKSYFK
     WLLIFYILFT ACCSGYYYME VSKSFVHPMY DVNSTLHVEG FKVIDKGVLR EIVPEDTCFS
     NKFVNFDAFW GRPYDNSRNC PIVTAVIDGD GTVATGVPGF VSWVMDGVMF IHMTQTERKP
     WYIPTWFNRE IVGYTQDSII TEGSFYTSIA LFSARCLYLT ASNTPQLYCF NGDNDAPGAL
     PFGSIIPHRV YFQPNGVRLI VPQQILHTPY VVKFVSDSYC RGSVCEYTRP GYCVSLNPQW
     VLFNDEYTSK PGVFCGSTVR ELMFSMVSTF FTGVNPNIYM QLATMFLILV VVVLIFAMVI
     KFQGVFKAYA TTVFITMLVW VINAFILCVH SYNSVLAVIL LVLYCYASLV TSRNTVIIMH
     CWLVFTFGLI VPTWLACCYL GFIIYMYTPL FLWCYGTTKN TRKLYDGNEF VGNYDLAAKS
     TFVIRGSEFV KLTNEIGDKF EAYLSAYARL KYYSGTGSEQ DYLQACRAWL AYALDQYRNS
     GVEIVYTPPR YSIGVSRLQS GFKKLVSPSS AVEKCIVSVS YRGNNLNGLW LGDTIYCPRH
     VLGKFSGDQW NDVLNLANNH EFEVTTQHGV TLNVVSRRLK GAVLILQTAV ANAETPKYKF
     IKANCGDSFT IACAYGGTVV GLYPVTMRSN GTIRASFLAG ACGSVGFNIE KGVVNFFYMH
     HLELPNALHT GTDLMGEFYG GYVDEEVAQR VPPDNLVTNN IVAWLYAAII SVKESSFSLP
     KWLESTTVSV DDYNKWAGDN GFTPFSTSTA ITKLSAITGV DVCKLLRTIM VKNSQWGGDP
     ILGQYNFEDE LTPESVFNQI GGVRLQSSFV RKATSWFWSR CVLACFLFVL CAIVLFTAVP
     LKFYVYAAVI LLMAVLFISF TVKHVMAYMD TFLLPTLITV IIGVCAEVPF IYNTLISQVV
     IFLSQWYDPV VFDTMVPWMF LPLVLYTAFK CVQGCYMNSF NTSLLMLYQF VKLGFVIYTS
     SNTLTAYTEG NWELFFELVH TTVLANVSSN SLIGLFVFKC AKWMLYYCNA TYLNNYVLMA
     VMVNCIGWLC TCYFGLYWWV NKVFGLTLGK YNFKVSVDQY RYMCLHKINP PKTVWEVFST
     NILIQGIGGD RVLPIATVQA KLSDVKCTTV VLMQLLTKLN VEANSKMHVY LVELHNKILA
     SDDVGECMDN LLGMLITLFC IDSTIDLSEY CDDILKRSTV LQSVTQEFSH IPSYAEYERA
     KNLYEKVLVD SKNGGVTQQE LAAYRKAANI AKSVFDRDLA VQKKLDSMAE RAMTTMYKEA
     RVTDRRAKLV SSLHALLFSM LKKIDSEKLN VLFDQASSGV VPLATVPIVC SNKLTLVIPD
     PETWVKCVEG VHVTYSTVVW NIDTVIDADG TELHPTSTGS GLTYCISGAN IAWPLKVNLT
     RNGHNKVDVV LQNNELMPHG VKTKACVAGV DQAHCSVESK CYYTNISGNS VVAAITSSNP
     NLKVASFLNE AGNQIYVDLD PPCKFGMKVG VKVEVVYLYF IKNTRSIVRG MVLGAISNVV
     VLQSKGHETE EVDAVGILSL CSFAVDPADT YCKYVAAGNQ PLGNCVKMLT VHNGSGFAIT
     SKPSPTPDQD SYGGASVCLY CRAHIAHPGS VGNLDGRCQF KGSFVQIPTT EKDPVGFCLR
     NKVCTVCQCW IGYGCQCDSL RQPKSSVQSV AGASDFDKNY LNRVRGSSEA RLIPLASGCD
     PDVVKRAFDV CNKESAGMFQ NLKRNCARFQ ELRDTEDGNL EYLDSYFVVK QTTPSNYEHE
     KSCYEDLKSE VTADHDFFVF NKNIYNISRQ RLTKYTMMDF CYALRHFDPK DCEVLKEILV
     TYGCIEDYHP KWFEENKDWY DPIENSKYYV MLAKMGPIVR RALLNAIEFG NLMVEKGYVG
     VITLDNQDLN GKFYDFGDFQ KTAPGAGVPV FDTYYSYMMP IIAMTDALAP ERYFEYDVHK
     GYKSYDLLKY DYTEEKQELF QKYFKYWDQE YHPNCRDCSD DRCLIHCANF NILFSTLIPQ
     TSFGNLCRKV FVDGVPFIAT CGYHSKELGV IMNQDNTMSF SKMGLSQLMQ FVGDPALLVG
     TSNNLVDLRT SCFSVCALTS GITHQTVKPG HFNKDFYDFA EKAGMFKEGS SIPLKHFFYP
     QTGNAAINDY DYYRYNRPTM FDICQLLFCL EVTSKYFECY EGGCIPASQV VVNNLDKSAG
     YPFNKFGKAR LYYEMSLEEQ DQLFEITKKN VLPTITQMNL KYAISAKNRA RTVAGVSILS
     TMTNRQFHQK ILKSIVNTRN ASVVIGTTKF YGGWDNMLRN LIQGVEDPIL MGWDYPKCDR
     AMPNLLRIAA SLVLARKHTN CCSWSERIYR LYNECAQVLS ETVLATGGIY VKPGGTSSGD
     ATTAYANSVF NIIQATSANV ARLLSVITRD IVYDNIKSLQ YELYQQVYRR VNFDPAFVEK
     FYSYLCKNFS LMILSDDGVV CYNNTLAKQG LVADISGFRE VLYYQNNVFM ADSKCWVEPD
     LEKGPHEFCS QHTMLVEVDG EPKYLPYPDP SRILGACVFV DDVDKTEPVA VMERYIALAI
     DAYPLVHHEN EEYKKVFFVL LAYIRKLYQE LSQNMLMDYS FVMDIDKGSK FWEQEFYENM
     YRAPTTLQSC GVCVVCNSQT ILRCGNCIRK PFLCCKCCYD HVMHTDHKNV LSINPYICSQ
     LGCGEADVTK LYLGGMSYFC GNHKPKLSIP LVSNGTVFGI YRANCAGSEN VDDFNQLATT
     NWSIVEPYIL ANRCSDSLRR FAAETVKATE ELHKQQFASA EVREVFSDRE LILSWEPGKT
     RPPLNRNYVF TGYHFTRTSK VQLGDFTFEK GEGKDVVYYK ATSTAKLSVG DIFVLTSHNV
     VSLVAPTLCP QQTFSRFVNL RPNVMVPECF VNNIPLYHLV GKQKRTTVQG PPGSGKSHFA
     IGLAVYFSSA RVVFTACSHA AVDALCEKAF KFLKVDDCTR IVPQRTTVDC FSKFKANDTG
     KKYIFSTINA LPEVSCDILL VDEVSMLTNY ELSFINGKIN YQYVVYVGDP AQLPAPRTLL
     NGSLSPKDYN VVTNLMVCVK PDIFLAKCYR CPKEIVDTVS TLVYDGKFIA NNPESRECFK
     VIVNNGNSDV GHESGSAYNT TQLEFVKDFV CRNKQWREAI FISPYNAMNQ RAYRMLGLNV
     QTVDSSQGSE YDYVIFCVTA DSQHALNINR FNVALTRAKR GILVVMRQRD ELYSALKFTE
     LDSETSLQGT GLFKICNKEF SGVHPAYAVT TKALAATYKV NDELAALVNV EAGSEITYKH
     LISLLGFKMS VNVEGCHNMF ITRDEAIRNV RGWVGFDVEA THACGTNIGT NLPFQVGFST
     GADFVVTPEG LVDTSIGNNF EPVNSKAPPG EQFNHLRVLF KSAKPWHVIR PRIVQMLADN
     LCNVSDCVVF VTWCHGLELT TLRYFVKIGK EQVCSCGSRA TTFNSHTQAY ACWKHCLGFD
     FVYNPLLVDI QQWGYSGNLQ FNHDLHCNVH GHAHVASVDA IMTRCLAINN AFCQDVNWDL
     TYPHIANEDE VNSSCRYLQR MYLNACVDAL KVNVVYDIGN PKGIKCVRRG DVNFRFYDKN
     PIVRNVKQFE YDYNQHKDKF ADGLCMFWNC NVDCYPDNSL VCRYDTRNLS VFNLPGCNGG
     SLYVNKHAFY TPKFDRISFR NLKAMPFFFY DSSPCETIQV DGVAQDLVSL ATKDCITKCN
     IGGAVCKKHA QMYAEFVTSY NAAVTAGFTF WVTNKLNPYN LWKSFSALQS IDNIAYNMYK
     GGHYDAIAGE MPTVITGDKV FVIDQGVEKA VFVNQTTLPT SVAFELYAKR NIRTLPNNRI
     LKGLGVDVTN GFVIWDYANQ TPLYRNTVKV CAYTDIEPNG LVVLYDDRYG DYQSFLAADN
     AVLVSTQCYK RYSYVEIPSN LLVQNGMPLK DGANLYVYKR VNGAFVTLPN TINTQGRSYE
     TFEPRSDIER DFLAMSEESF VERYGKDLGL QHILYGEVDK PQLGGLHTVI GMYRLLRANK
     LNAKSVTNSD SDVMQNYFVL SDNGSYKQVC TVVDLLLDDF LELLRNILKE YGTNKSKVVT
     VSIDYHSINF MTWFEDGSIK TCYPQLQSAW TCGYNMPELY KVQNCVMEPC NIPNYGVGIT
     LPSGILMNVA KYTQLCQYLL KTTICVPHNM RVMHFGAGSD KGVAPGSTVL KQWLPEGTLL
     VDNDIVDYVS DAHVSVLSDC NKYNTEHKFD LVISDMYTDN DSKRKHEGVI ANNGNDDVFI
     YLSSFLRNNL ALGGSFAVKV TETSWHEVLY DIAQDCAWWT MFCTAVNASS SEAFLIGVNY
     LGASEKVKVS GKTLHANYIF WRNCNYLQTS AYSIFDVAKF DLRLKATPVV NLKTEQKTDL
     VFNLIKCGKL LVRDVGNTSF TSDSFVCTM
 
 
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